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Showing Protein S-methyl-5'-thioadenosine phosphorylase (HMDBP00397)

IdentificationBiological propertiesGene propertiesProtein propertiesExternal linksReferencesXMLShow 9 metabolites
Identification
HMDB Protein ID HMDBP00397
Secondary Accession Numbers
  • 5634
Name S-methyl-5'-thioadenosine phosphorylase
Synonyms
  1. 5'-methylthioadenosine phosphorylase
  2. MTA phosphorylase
  3. MTAPase
  4. MTAP
Gene Name MTAP
Protein Type Enzyme
Biological Properties
General Function Involved in transferase activity, transferring pentosyl groups
Specific Function Catalyzes the reversible phosphorylation of S-methyl-5'-thioadenosine (MTA) to adenine and 5-methylthioribose-1-phosphate. Involved in the breakdown of MTA, a major by-product of polyamine biosynthesis. Responsible for the first step in the methionine salvage pathway after MTA has been generated from S-adenosylmethionine. Has broad substrate specificity with 6-aminopurine nucleosides as preferred substrates.
Pathways
  • Cystathionine Beta-Synthase Deficiency
  • Cysteine and methionine metabolism
  • Glycine N-methyltransferase Deficiency
  • Homocystinuria-megaloblastic anemia due to defect in cobalamin metabolism, cblG complementation type
  • Hypermethioninemia
  • L-methionine biosynthesis via salvage pathway
  • Methionine Adenosyltransferase Deficiency
  • Methionine Metabolism
  • Methylenetetrahydrofolate Reductase Deficiency (MTHFRD)
  • S-Adenosylhomocysteine (SAH) Hydrolase Deficiency
Reactions
5'-Methylthioadenosine + Phosphate → Adenine + 5-Methylthioribose 1-phosphate details
GO Classification
Biological Process
purine ribonucleoside salvage
L-methionine salvage from methylthioadenosine
polyamine metabolic process
nucleobase-containing compound metabolic process
Cellular Component
cytosol
nucleus
Function
catalytic activity
transferase activity
transferase activity, transferring pentosyl groups
transferase activity, transferring glycosyl groups
Molecular Function
phosphorylase activity
S-methyl-5-thioadenosine phosphorylase activity
Process
metabolic process
nitrogen compound metabolic process
cellular nitrogen compound metabolic process
nucleobase, nucleoside, nucleotide and nucleic acid metabolic process
nucleobase, nucleoside and nucleotide metabolic process
nucleoside metabolic process
Cellular Location
  1. Cytoplasm
Gene Properties
Chromosome Location 9
Locus 9p21
SNPs MTAP
Gene Sequence 
>852 bp
ATGGCCTCTGGCACCACCACCACCGCCGTGAAGATTGGAATAATTGGTGGAACAGGCCTG
GATGATCCAGAAATTTTAGAAGGAAGAACTGAAAAATATGTGGATACTCCATTTGGCAAG
CCATCTGATGCCTTAATTTTGGGGAAGATAAAAAATGTTGATTGCATCCTCCTTGCAAGG
CATGGAAGGCAGCACACCATCATGCCTTCAAAGGTCAACTACCAGGCGAACATCTGGGCT
TTGAAGGAAGAGGGCTGTACACATGTCATAGTGACCACAGCTTGTGGCTCCTTGAGGGAG
GAGATTCAGCCCGGCGATATTGTCATTATTGATCAGTTCATTGACAGGACCACTATGAGA
CCTCAGTCCTTCTATGATGGAAGTCATTCTTGTGCCAGAGGAGTGTGCCATATTCCAATG
GCTGAGCCGTTTTGCCCCAAAACGAGAGAGGTTCTTATAGAGACTGCTAAGAAGCTAGGA
CTCCGGTGCCACTCAAAGGGGACAATGGTCACAATCGAGGGACCTCGTTTTAGCTCCCGG
GCAGAAAGCTTCATGTTCCGCACCTGGGGGGCGGATGTTATCAACATGACCACAGTTCCA
GAGGTGGTTCTTGCTAAGGAGGCTGGAATTTGTTACGCAAGTATCGCCATGGCGACAGAT
TATGACTGCTGGAAGGAGCACGAGGAAGCAGTTTCGGTGGACCGGGTCTTAAAGACCCTG
AAAGAAAACGCTAATAAAGCCAAAAGCTTACTGCTCACTACCATACCTCAGATAGGGTCC
ACAGAATGGTCAGAAACCCTCCATAACCTGAAGAATATGGCCCAGTTTTCTGTTTTATTA
CCAAGACATTAA
Protein Properties
Number of Residues 283
Molecular Weight 31235.76
Theoretical pI 7.188
Pfam Domain Function
Signals Not Available
Transmembrane Regions Not Available
Protein Sequence 
>S-methyl-5'-thioadenosine phosphorylase
MASGTTTTAVKIGIIGGTGLDDPEILEGRTEKYVDTPFGKPSDALILGKIKNVDCVLLAR
HGRQHTIMPSKVNYQANIWALKEEGCTHVIVTTACGSLREEIQPGDIVIIDQFIDRTTMR
PQSFYDGSHSCARGVCHIPMAEPFCPKTREVLIETAKKLGLRCHSKGTMVTIEGPRFSSR
AESFMFRTWGADVINMTTVPEVVLAKEAGICYASIAMATDYDCWKEHEEAVSVDRVLKTL
KENANKAKSLLLTTIPQIGSTEWSETLHNLKNMAQFSVLLPRH
GenBank ID Protein 847724
UniProtKB/Swiss-Prot ID Q13126
UniProtKB/Swiss-Prot Entry Name MTAP_HUMAN
PDB IDs
GenBank Gene ID U22233
GeneCard ID MTAP
GenAtlas ID MTAP
HGNC ID HGNC:7413
References
General References
  1. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed:15489334 ]
  2. Beausoleil SA, Jedrychowski M, Schwartz D, Elias JE, Villen J, Li J, Cohn MA, Cantley LC, Gygi SP: Large-scale characterization of HeLa cell nuclear phosphoproteins. Proc Natl Acad Sci U S A. 2004 Aug 17;101(33):12130-5. Epub 2004 Aug 9. [PubMed:15302935 ]
  3. Gauci S, Helbig AO, Slijper M, Krijgsveld J, Heck AJ, Mohammed S: Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach. Anal Chem. 2009 Jun 1;81(11):4493-501. doi: 10.1021/ac9004309. [PubMed:19413330 ]
  4. Humphray SJ, Oliver K, Hunt AR, Plumb RW, Loveland JE, Howe KL, Andrews TD, Searle S, Hunt SE, Scott CE, Jones MC, Ainscough R, Almeida JP, Ambrose KD, Ashwell RI, Babbage AK, Babbage S, Bagguley CL, Bailey J, Banerjee R, Barker DJ, Barlow KF, Bates K, Beasley H, Beasley O, Bird CP, Bray-Allen S, Brown AJ, Brown JY, Burford D, Burrill W, Burton J, Carder C, Carter NP, Chapman JC, Chen Y, Clarke G, Clark SY, Clee CM, Clegg S, Collier RE, Corby N, Crosier M, Cummings AT, Davies J, Dhami P, Dunn M, Dutta I, Dyer LW, Earthrowl ME, Faulkner L, Fleming CJ, Frankish A, Frankland JA, French L, Fricker DG, Garner P, Garnett J, Ghori J, Gilbert JG, Glison C, Grafham DV, Gribble S, Griffiths C, Griffiths-Jones S, Grocock R, Guy J, Hall RE, Hammond S, Harley JL, Harrison ES, Hart EA, Heath PD, Henderson CD, Hopkins BL, Howard PJ, Howden PJ, Huckle E, Johnson C, Johnson D, Joy AA, Kay M, Keenan S, Kershaw JK, Kimberley AM, King A, Knights A, Laird GK, Langford C, Lawlor S, Leongamornlert DA, Leversha M, Lloyd C, Lloyd DM, Lovell J, Martin S, Mashreghi-Mohammadi M, Matthews L, McLaren S, McLay KE, McMurray A, Milne S, Nickerson T, Nisbett J, Nordsiek G, Pearce AV, Peck AI, Porter KM, Pandian R, Pelan S, Phillimore B, Povey S, Ramsey Y, Rand V, Scharfe M, Sehra HK, Shownkeen R, Sims SK, Skuce CD, Smith M, Steward CA, Swarbreck D, Sycamore N, Tester J, Thorpe A, Tracey A, Tromans A, Thomas DW, Wall M, Wallis JM, West AP, Whitehead SL, Willey DL, Williams SA, Wilming L, Wray PW, Young L, Ashurst JL, Coulson A, Blocker H, Durbin R, Sulston JE, Hubbard T, Jackson MJ, Bentley DR, Beck S, Rogers J, Dunham I: DNA sequence and analysis of human chromosome 9. Nature. 2004 May 27;429(6990):369-74. [PubMed:15164053 ]
  5. Olopade OI, Pomykala HM, Hagos F, Sveen LW, Espinosa R 3rd, Dreyling MH, Gursky S, Stadler WM, Le Beau MM, Bohlander SK: Construction of a 2.8-megabase yeast artificial chromosome contig and cloning of the human methylthioadenosine phosphorylase gene from the tumor suppressor region on 9p21. Proc Natl Acad Sci U S A. 1995 Jul 3;92(14):6489-93. [PubMed:7604019 ]
  6. Nobori T, Takabayashi K, Tran P, Orvis L, Batova A, Yu AL, Carson DA: Genomic cloning of methylthioadenosine phosphorylase: a purine metabolic enzyme deficient in multiple different cancers. Proc Natl Acad Sci U S A. 1996 Jun 11;93(12):6203-8. [PubMed:8650244 ]
  7. Della Ragione F, Takabayashi K, Mastropietro S, Mercurio C, Oliva A, Russo GL, Della Pietra V, Borriello A, Nobori T, Carson DA, Zappia V: Purification and characterization of recombinant human 5'-methylthioadenosine phosphorylase: definite identification of coding cDNA. Biochem Biophys Res Commun. 1996 Jun 25;223(3):514-9. [PubMed:8687427 ]
  8. Appleby TC, Erion MD, Ealick SE: The structure of human 5'-deoxy-5'-methylthioadenosine phosphorylase at 1.7 A resolution provides insights into substrate binding and catalysis. Structure. 1999 Jun 15;7(6):629-41. [PubMed:10404592 ]